Purification and characterization of a new aldehyde oxidase from pseudomonas sp. AIU 362.
An aldehyde oxidase exhibiting high activity on glyoxal was purified to an electrophoretically homogenous state from Pseudomonas sp. AIU 362, which was isolated from a soil sample using a methoxyethanol medium. The enzyme oxidized not only glyoxal but also short-chain aliphatic aldehydes and aromatic aldehydes. Thus, this enzyme was classified into the aldehyde oxidase (ALOD) group. However, it was composed of four identical subunits with a molecular mass of 27 kDa, whereas other microbial ALODs were composed of three hetero subunits, and ALODs from plant and animals were composed of two identical subunits. The NH(2)-terminal sequence also showed no similarity to that of other ALODs. These results indicate that ALOD from Pseudomonas sp. AIU 362 is a new aldehyde oxidase. This ALOD was induced by 2-methoxyethanol, methanol or isopropanol.
Sasaki
Yasutaka
Y
The United Graduate School of Agricultural Sciences, Iwate University, 18-8 Ueda 3- chome, Morioka 020-8550, Japan.
Isobe
Kimiyasu
K
Kataoka
Michihiko
M
Ogawa
Jun
J
Iwasaki
Akira
A
Hasegawa
Junzo
J
Shimizu
Sakayu
S
D042931:Aldehyde Oxidase / Q000737:chemistry* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D004789:Enzyme Activation; D004795:Enzyme Stability; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011549:Pseudomonas / Q000145:classification* / Q000201:enzymology*; D012988:Soil Microbiology; D013045:Species Specificity
D042931:Aldehyde Oxidase